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Database: UniProt/TrEMBL
Entry: F4CY30_PSEUX
LinkDB: F4CY30_PSEUX
Original site: F4CY30_PSEUX 
ID   F4CY30_PSEUX            Unreviewed;       466 AA.
AC   F4CY30;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   25-OCT-2017, entry version 38.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   OrderedLocusNames=Psed_2046 {ECO:0000313|EMBL:AEA24271.1};
OS   Pseudonocardia dioxanivorans (strain ATCC 55486 / DSM 44775 / JCM
OS   13855 / CB1190).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Pseudonocardia.
OX   NCBI_TaxID=675635 {ECO:0000313|EMBL:AEA24271.1, ECO:0000313|Proteomes:UP000007809};
RN   [1] {ECO:0000313|EMBL:AEA24271.1, ECO:0000313|Proteomes:UP000007809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 55486 / DSM 44775 / JCM 13855 / CB1190
RC   {ECO:0000313|Proteomes:UP000007809};
RX   PubMed=21725009; DOI=10.1128/JB.00415-11;
RA   Sales C.M., Mahendra S., Grostern A., Parales R.E., Goodwin L.A.,
RA   Woyke T., Nolan M., Lapidus A., Chertkov O., Ovchinnikova G.,
RA   Sczyrba A., Alvarez-Cohen L.;
RT   "Genome sequence of the 1,4-dioxane-degrading Pseudonocardia
RT   dioxanivorans strain CB1190.";
RL   J. Bacteriol. 193:4549-4550(2011).
CC   -!- CATALYTIC ACTIVITY: L-glutamate = 4-aminobutanoate + CO(2).
CC       {ECO:0000256|RuleBase:RU361171}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC         ECO:0000256|RuleBase:RU361171};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU361171}.
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DR   EMBL; CP002593; AEA24271.1; -; Genomic_DNA.
DR   RefSeq; WP_013674202.1; NC_015312.1.
DR   STRING; 675635.Psed_2046; -.
DR   EnsemblBacteria; AEA24271; AEA24271; Psed_2046.
DR   KEGG; pdx:Psed_2046; -.
DR   eggNOG; ENOG4105CVK; Bacteria.
DR   eggNOG; COG0076; LUCA.
DR   KO; K01580; -.
DR   OrthoDB; POG091H06F5; -.
DR   Proteomes; UP000007809; Chromosome.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006536; P:glutamate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR010107; Glutamate_decarboxylase.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   PANTHER; PTHR43321; PTHR43321; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01788; Glu-decarb-GAD; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000007809};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU361171, ECO:0000313|EMBL:AEA24271.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007809}.
FT   MOD_RES     274    274       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   466 AA;  51770 MW;  D26CE39EB1F7EFB0 CRC64;
     MPLHDRDTVR DELDDCVFVD RDLTRPVTKY RFPQEESLPR DVSQLVSDEL MLDGNARQNL
     ATFCQTWVEP EVMGLMALSV SKNMIDKDEY PQTAEIERRC VHMMADLWNA PEAANTVGAS
     AIGSSEACML AGMAAKWRWR AKRRAAGKPV DNPNMVCGPV QVVWHKFARY WDIEMREVPM
     APGSYAMDAA SMLERVDENT IMVVPTLGVT YTGAYEPVAD MALALDQLQA DTGLDVDIHV
     DAASGGFLAP FCAPDLAFDF RLPRVKSISA SGHKFGLAPL GVGWVVWRGA GELPDDLVFH
     VNYLGGDMPV FQINFSRPAG QIVASYYNFL RLGREGYRRI HDASYDVGQY LAAEIVKLGP
     FELLCDSRPD TGIPTVTWRI REGEDPGYTL YDLADRLRTK GWQVPAYTLT GTASDIAVQR
     ILVRLGVSRD MASLLLDDFR DAVAHFGKHP VTIPMTKQES GGFSHL
//
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